Abstract
The carotid body contains enkephalins and tachykinins1–3. Several studies have shown that these peptides may be of importance in chemoreception3–6. Mechanisms that regulate the levels of these peptides in the carotid body have not been studied. Generally, neuropeptides are degraded by specific proteases7. The enzyme-neutral endopeptidase (also called enkephalinase (E.C.3.4.24.11)) is involved in the metabolism of ekephalins and tachykinins in the brain and kidney7,8.
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I. V. Chen, R. D. Yates, and J. T. Hansen, Substance P-like immuno- reactivity in rat and cat carotid bodies: Light and electron microscopic studies, Histol. Histopathol. 1:203 (1986).
J. Wharton, J. M. Polak, A. G. E. Pearse, G. P. McGregor, M. G. Bryant, S. R. Bloom, P. C. Emson, G. E. Bisgard, and J. A. Will, Enkephalin-, VIP-, and substance P-like immunoreactivity in the carotid body. Nature 284:269 (1980).
N. R. Prabhakar, S. C. Landis, G. K. Kumar, D. Mullikin-Kilpatrick, N. S. Cherniack, and S. E. Leeman, Substance P and neurokinin A in the cat carotid body: localization, exogenous effects and changes in content in response to arterial PO2, Brain Res. 481:205 (1989).
S. Pidone and C. Gonzalez, Initiation and control of chemoreceptor activity in the carotid body, in: “Handbook of Physiology, Sect. 3, The Respiratory System, Vol II,” N. S. Cherniack and J. G. Widdicombe, eds.. Am. Physiological Society, Bethesda (1986).
L. Monti-Bloch and C. Eyzaguirre, Effects of methionine-enkephalin and substance P on the chemosensory discharge of the cat carotid body. Brain Res. 338:297 (1985).
N. R. Prabhakar, M. Runold, Y. Yamamoto, H. Lagergrantz, and C. Von Euler, Effect of substance P antagonist on the hypoxic induced carotid chemoreceptor activity. Acta Physiol. Scand. 121:301 (1984).
A. J. Turner, N. M. Hooper, and A. J. Kenny, Metabolism of neuropeptides, in: “Mammalian Ectoenzymes,” A. J. Kenny and A. J. Turner, eds., Elsevier, Amsterdam (1987).
A. J. Turner, Endopeptidase-24.11 and neuropeptide metabolism, in; “Neuropeptides and their Peptidases,” A. J. Turner, ed., Ellis- Horwood, Chichester (1987).
T. Maeda, K. Balakrishnan, and S. Q. Mehdi, A simple and rapid method for the preparation of plasma membranes, Biochim. Biophys. Acta 731:115 (1983).
M. Orlowski and S. Wilk, Purification and specificity of a membrane bound metalloendopeptidase from bovine pituitary. Biochemistry 20: 4942 (1981).
J. I. Elliot and J. M. Brewer, The inactivation of yeast enolase by 2,3-butanedione, Arch. Biochem. Biophys. 190:351 (1978).
E. G. Erdos and R. A. Skidgel, Neutral endopeptidase 24.11 (enkepha-linase) and related regulators of peptide hormones, FASEB J. 3:145 (1989).
A. Molteni, R. M. Zakheim, K. B. Mullis, and L. Mattioli, The effect of chronic alveolar hypoxia on lung and serum angiotensin I converting enzyme activity, Proc. Soc. Exp. Biol. Med. 147:263 (1974).
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© 1990 Plenum Press, New York
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Kumar, G.K., Cherniack, N.S., Prabhakar, N.R. (1990). Biochemical Analysis of Neutral Endopeptidase Activity of the Cat Carotid Body. In: Acker, H., Trzebski, A., O’Regan, R.G. (eds) Chemoreceptors and Chemoreceptor Reflexes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8938-5_15
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DOI: https://doi.org/10.1007/978-1-4684-8938-5_15
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